Structure of PDB 4n09 Chain C

Receptor sequence
>4n09C (length=345) [Search protein sequence]
MSSAPLRVYVQCNPLLDVSAHVSDEFLVKYGLERGTAILLSERQKGIFDD
IEKMPNVRYVPGGSGLNVARVAQWMQQAYKGKFVTYVGCIADDRYGKVLK
EAAEHEGIVMAVEHTTKAGSGACAVCITGKERTLVADLGAANHLSSEHMR
SPAVVRAMDESRIFYFSGFTLTVDVNHVLQACRKAREVDGLFMINLSAPF
IMQFFSAQLGEVLPYTDIIVANRHEAKEFANMMKWDTDCVEEIARRAVSE
VPYTGTKGRVVVFTRDIESTVLATKDGVETVPVPQLDQDKVIDMNGAGDA
FMGGFLSAYAVGKDLRRCCETGHYTAQEVIQRDGCSFPEKPSFSP
3D structure
PDB4n09 Structures of adenosine kinase from Trypanosoma brucei brucei.
ChainC
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R132 D299
Catalytic site (residue number reindexed from 1) R132 D299
Enzyme Commision number 2.7.1.20: adenosine kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADN C N13 L15 D17 G63 S64 N67 C123 A136 F169 D299 N13 L15 D17 G63 S64 N67 C123 A136 F169 D299
BS02 ADP C N222 T264 D266 I267 V283 Q288 G298 H323 A326 Q327 I330 N222 T264 D266 I267 V283 Q288 G298 H323 A326 Q327 I330
Gene Ontology
Molecular Function
GO:0004001 adenosine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0006144 purine nucleobase metabolic process
GO:0006166 purine ribonucleoside salvage
GO:0009152 purine ribonucleotide biosynthetic process
GO:0016310 phosphorylation
GO:0044209 AMP salvage
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0020015 glycosome
GO:0097014 ciliary plasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4n09, PDBe:4n09, PDBj:4n09
PDBsum4n09
PubMed24419613
UniProtQ584S0

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